Local view for "http://wifo5-04.informatik.uni-mannheim.de/drugbank/resource/drugs/DB08422"
| Predicate | Value (sorted: none) |
|---|---|
| rdf:type | |
| rdfs:label |
"[PHENYLALANINYL-PROLINYL]-[2-(PYRIDIN-4-YLAMINO)-ETHYL]-AMINE"
|
| ns1:description |
"
experimental
This compound belongs to the peptides. These are compounds containing an amide derived from two or more amino carboxylic acid molecules (the same or different) by formation of a covalent bond from the carbonyl carbon of one to the nitrogen atom of another.
Peptides
Organic Compounds
Organic Acids and Derivatives
Carboxylic Acids and Derivatives
Amino Acids, Peptides, and Analogues
Alpha Amino Acid Amides
Phenylpropylamines
Amphetamines and Derivatives
Pyrrolidinecarboxamides
Aminopyridines and Derivatives
Tertiary Carboxylic Acid Amides
Secondary Carboxylic Acid Amides
Tertiary Amines
Carboxylic Acids
Enolates
Polyamines
Secondary Amines
Monoalkylamines
alpha-amino acid amide
alpha-amino acid or derivative
amphetamine or derivative
phenylpropylamine
pyrrolidine carboxylic acid or derivative
pyrrolidine-2-carboxamide
aminopyridine
pyridine
benzene
pyrrolidine
tertiary carboxylic acid amide
carboxamide group
secondary carboxylic acid amide
tertiary amine
polyamine
secondary amine
enolate
carboxylic acid
amine
primary aliphatic amine
primary amine
organonitrogen compound
logP
0.99
ALOGPS
logS
-3.4
ALOGPS
Water Solubility
1.72e-01 g/l
ALOGPS
logP
0.29
ChemAxon
IUPAC Name
(2S)-1-[(2R)-2-amino-3-phenylpropanoyl]-N-{2-[(pyridin-4-yl)amino]ethyl}pyrrolidine-2-carboxamide
ChemAxon
Traditional IUPAC Name
(2S)-1-[(2R)-2-amino-3-phenylpropanoyl]-N-[2-(pyridin-4-ylamino)ethyl]pyrrolidine-2-carboxamide
ChemAxon
Molecular Weight
381.4714
ChemAxon
Monoisotopic Weight
381.216475133
ChemAxon
SMILES
[H][C@@](N)(CC1=CC=CC=C1)C(=O)N1CCC[C@@]1([H])C(=O)NCCNC1=CC=NC=C1
ChemAxon
Molecular Formula
C21H27N5O2
ChemAxon
InChI
InChI=1S/C21H27N5O2/c22-18(15-16-5-2-1-3-6-16)21(28)26-14-4-7-19(26)20(27)25-13-12-24-17-8-10-23-11-9-17/h1-3,5-6,8-11,18-19H,4,7,12-15,22H2,(H,23,24)(H,25,27)/t18-,19+/m1/s1
ChemAxon
InChIKey
InChIKey=GEIDRYBJURDUSW-MOPGFXCFSA-N
ChemAxon
Polar Surface Area (PSA)
100.35
ChemAxon
Refractivity
108.95
ChemAxon
Polarizability
40.54
ChemAxon
Rotatable Bond Count
8
ChemAxon
H Bond Acceptor Count
5
ChemAxon
H Bond Donor Count
3
ChemAxon
pKa (strongest acidic)
15.29
ChemAxon
pKa (strongest basic)
8.86
ChemAxon
Physiological Charge
2
ChemAxon
Number of Rings
3
ChemAxon
Bioavailability
1
ChemAxon
Rule of Five
true
ChemAxon
Ghose Filter
true
ChemAxon
MDDR-Like Rule
true
ChemAxon
PubChem Compound
23586040
PubChem Substance
99444893
PDB
PPX
BE0000048
Prothrombin
Human
# Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235
unknown
Prothrombin
Involved in blood clotting cascade
Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C
F2
11p11-q12
Secreted protein; extracellular space
None
5.7
70037.0
Human
HUGO Gene Nomenclature Committee (HGNC)
HGNC:3535
GenAtlas
F2
GeneCards
F2
GenBank Gene Database
M17262
GenBank Protein Database
339641
UniProtKB
P00734
UniProt Accession
THRB_HUMAN
Activated Factor II [IIa]
Coagulation factor II
EC 3.4.21.5
Prothrombin precursor
Thrombin
>Prothrombin precursor
MAHVRGLQLPGCLALAALCSLVHSQHVFLAPQQARSLLQRVRRANTFLEEVRKGNLEREC
VEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHV
NITRSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQE
CSIPVCGQDQVTVAMTPRSEGSSVNLSPPLEQCVPDRGQQYQGRLAVTTHGLPCLAWASA
QAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAVEEETG
DGLDEDSDRAIEGRTATSEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYI
DGRIVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTEN
DLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHP
VCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDST
RIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKY
GFYTHVFRLKKWIQKVIDQFGE
>1869 bp
ATGGCGCACGTCCGAGGCTTGCAGCTGCCTGGCTGCCTGGCCCTGGCTGCCCTGTGTAGC
CTTGTGCACAGCCAGCATGTGTTCCTGGCTCCTCAGCAAGCACGGTCGCTGCTCCAGCGG
GTCCGGCGAGCCAACACCTTCTTGGAGGAGGTGCGCAAGGGCAACCTAGAGCGAGAGTGC
GTGGAGGAGACGTGCAGCTACGAGGAGGCCTTCGAGGCTCTGGAGTCCTCCACGGCTACG
GATGTGTTCTGGGCCAAGTACACAGCTTGTGAGACAGCGAGGACGCCTCGAGATAAGCTT
GCTGCATGTCTGGAAGGTAACTGTGCTGAGGGTCTGGGTACGAACTACCGAGGGCATGTG
AACATCACCCGGTCAGGCATTGAGTGCCAGCTATGGAGGAGTCGCTACCCACATAAGCCT
GAAATCAACTCCACTACCCATCCTGGGGCCGACCTACAGGAGAATTTCTGCCGCAACCCC
GACAGCAGCACCACGGGACCCTGGTGCTACACTACAGACCCCACCGTGAGGAGGCAGGAA
TGCAGCATCCCTGTCTGTGGCCAGGATCAAGTCACTGTAGCGATGACTCCACGCTCCGAA
GGCTCCAGTGTGAATCTGTCACCTCCATTGGAGCAGTGTGTCCCTGATCGGGGGCAGCAG
TACCAGGGGCGCCTGGCGGTGACCACACATGGGCTCCCCTGCCTGGCCTGGGCCAGCGCA
CAGGCCAAGGCCCTGAGCAAGCACCAGGACTTCAACTCAGCTGTGCAGCTGGTGGAGAAC
TTCTGCCGCAACCCAGACGGGGATGAGGAGGGCGTGTGGTGCTATGTGGCCGGGAAGCCT
GGCGACTTTGGGTACTGCGACCTCAACTATTGTGAGGAGGCCGTGGAGGAGGAGACAGGA
GATGGGCTGGATGAGGACTCAGACAGGGCCATCGAAGGGCGTACCGCCACCAGTGAGTAC
CAGACTTTCTTCAATCCGAGGACCTTTGGCTCGGGAGAGGCAGACTGTGGGCTGCGACCT
CTGTTCGAGAAGAAGTCGCTGGAGGACAAAACCGAAAGAGAGCTCCTGGAATCCTACATC
GACGGGCGCATTGTGGAGGGCTCGGATGCAGAGATCGGCATGTCACCTTGGCAGGTGATG
CTTTTCCGGAAGAGTCCCCAGGAGCTGCTGTGTGGGGCCAGCCTCATCAGTGACCGCTGG
GTCCTCACCGCCGCCCACTGCCTCCTGTACCCGCCCTGGGACAAGAACTTCACCGAGAAT
GACCTTCTGGTGCGCATTGGCAAGCACTCCCGCACAAGGTACGAGCGAAACATTGAAAAG
ATATCCATGTTGGAAAAGATCTACATCCACCCCAGGTACAACTGGCGGGAGAACCTGGAC
CGGGACATTGCCCTGATGAAGCTGAAGAAGCCTGTTGCCTTCAGTGACTACATTCACCCT
GTGTGTCTGCCCGACAGGGAGACGGCAGCCAGCTTGCTCCAGGCTGGATACAAGGGGCGG
GTGACAGGCTGGGGCAACCTGAAGGAGACGTGGACAGCCAACGTTGGTAAGGGGCAGCCC
AGTGTCCTGCAGGTGGTGAACCTGCCCATTGTGGAGCGGCCGGTCTGCAAGGACTCCACC
CGGATCCGCATCACTGACAACATGTTCTGTGCTGGTTACAAGCCTGATGAAGGGAAACGA
GGGGATGCCTGTGAAGGTGACAGTGGGGGACCCTTTGTCATGAAGAGCCCCTTTAACAAC
CGCTGGTATCAAATGGGCATCGTCTCATGGGGTGAAGGCTGTGACCGGGATGGGAAATAT
GGCTTCTACACACATGTGTTCCGCCTGAAGAAGTGGATACAGAAGGTCATTGATCAGTTT
GGAGAGTAG
PF00594
Gla
PF00051
Kringle
PF00089
Trypsin
component
extracellular region
function
catalytic activity
function
thrombin activity
function
hydrolase activity
function
calcium ion binding
function
peptidase activity
function
ion binding
function
endopeptidase activity
function
cation binding
function
serine-type endopeptidase activity
function
binding
process
blood coagulation
process
metabolism
process
macromolecule metabolism
process
protein metabolism
process
proteolysis
process
cellular protein metabolism
process
organismal physiological process
process
regulation of body fluids
process
physiological process
process
hemostasis
"
|
All properties reside in the graph file:///home/swish/src/ClioPatria/guidelines/drugbank_small.nt
The resource does not appear as an object